Mr. Bibo analyzed a mixture of amino acids using thin layer chromatography where the stationaryphase is a silica-coated plate. For the mobile phase, he used 50% ethyl acetate in hexane. Themixture contained three (3) amino acids whose structures are shown below.HO.HONH2HO,HO.NH2NH2PhenylalanineThreonineAspartic acida.) From the amino acids listed above, identify spots A, B, C, and D in the chromatogram below.BOCOb.) Threonine can be phosphorylated using an enzyme called protein kinase. The reaction is shownbelow. Given the same conditions Mr. Bibo used in his analysis, will the phosphorylated threoninehave a higher, smaller, or the same Rf value compared to threonine? Explain in one sentence.АТРADPCH3CH3Protein kinaseононNH2NH2ThreoninePhosphorylated threonine

Thin Layer Chromatography is an analytical technique which is used for analysis of mixture on the…

Answered: Mr. Bibo analyzed a mixture of amino…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Similar questions

1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
Name the compound: 1. Lys-Ile-Met-Val Draw the forms of the amino acid in the solution. 2. Glutamic Acid (4 forms) 3. Lysine (4 forms)
Answer the questions regarding the tripeptide shown. H3N-CH- -C N-CH-C-N-CH-C-O | CH СНОН H CH2 H3C CH3 CH3 SH Which amino acid is the C-terminal amino acid? threonine cysteine methionine valine What is the name'of this tripeptide, using the three-letter amino acid abbreviations? Capitalize the first let
Sample A may or may not contain amino acid/s. Based on the two tests performed, Sample D may or may not contain amino acid/s. Based on the two tests parformed, answer the Sample B may or may not contain amino acid/s. Based on the two tests performed, answer the atinne halnw answer the auestions below. auactinne helnw Xanthoproteic Pauly reaction Kanthoproteic Sample A Sample Sample D Mon's Milon's Xanihoproteic Identify the reactive functional group Interpret whether the result for each test is positive or negative for the presence of a certain amino acid. Interpret whether the result for each test is positive or negative for the presence of a certain amino acid. of the amino acid present responsible for the positive result/s. If there is NONE, choose "n/a" 1. Xanthoproteic test JA. Positive ,B Negative) 1. Xanthoproteic testJA. Positive , B Negative) 5. Xanthoproteic test 2. Millen's test (A Poaive B. Negetive) 2. Pauly ReactionA. Positive . 8. Nagative) 6. Millon'sst Identify the…
Lead Acetate Reaction To 1 mL of the sample in a test tube add 1 mL of 40% NaOH. Boil the content for at least 3 minutes. After cooling, add 2 – 3 drops of 10% Pb(OAc)2. Note the color of the solution or precipitate formed. Question 1. What happened to the proteins after adding 40% NaOH and heating the solution?Question 2. What specific amino acid is detected in this reaction?Question 3. What is the identity of the precipitate, if there is any?
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
An octapeptide was hydrolyzed and the amino acids separated. Its amino acid composition was determined: Gly (1); Ala (2); Val (1); Lys (2); Met (1); Asp (1). After incubation with FDNB and hydrolysis, 2,4-dinitrophenylalanine was detected. NO, H N -C- COOH H O,N CH, Treatment with cyanogen bromide, which cleaves at M, resulted in two fragments: a pentapeptide containing two K residues and a tripeptide containing V, G, and A. The residues are not listed in any particular order. After treatment with trypsin, which cleaves at R and K, there were three fragments: two dipeptides and MGAV. What is the sequence of the octapeptide? Use the one-letter abbreviations for the amino acids, and do not use dashes. octapeptide sequence:
A mixture of lipids containing phosphatidic acid, cholesterol, testosterone, phosphatidylserine, andphosphatidylethanolamine was applied to a hydrophobic interaction chromatography column. Thecolumn was washed with a high salt buffer, and the lipids were then eluted with decreasing saltconcentrations. In what order would the lipids be eluted from the column? Explain your answer.
Sucrose does not undergo mutarotation. Explain.
Is there a possibility for lactose to give a positive Mucic Acid test? Explain.
Inulin is a polysaccharide compound entirely of fructose units. What would be the effect of the seliwanoff's test on inulin? Explain in 2-3 sentences.
A mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase Transferrin

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS